Matrix metalloproteinases regulate neovascularization by acting as pericellular fibrinolysins

Article Abstract:

Fibrinolytic plasminogen activator (PA)-plasminogen system is not required for angiogenesis because tissues isolated from PA- or plasminogen-deficient mice neovascularize fibrin gels. In comparison, neovessel formation is dependent on fibrinolytic, endothelial cell-derived matrix metalloproteinases (MMP). MMPs regulate this process as invasion-incompetent cells penetrate fibrin barriers when transfected with a potent fibrinolytic MMP. These data identify a PA-independent fibrinolytic pathway wherein MMPs function as pericellular fibrinolysins during neovascularization.

Neovascularization, Metalloenzymes, Plasminogen activators, Fibrinolytic agents, Plasmin

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A cancer cell metalloprotease triad regulates the basement membrane transmigration program

Article Abstract:

The identification of a proteolytic triad that arms human cancer cells with the ability to transmigrate native basement membrane (BM) barriers are found to have important implications for the design of a new generation of selective, therapeutic interventions operative at the cell-matrix interface. Studies that have characterized the first series of gene products capable of orchestrating the entire BM remodeling program that distinguishes the carcinomatous phenotype are presented.

Pharmaceutical Preparation Manufacturing, Pharmaceutical preparations, Biological Product (except Diagnostic) Manufacturing, Drugs, Michigan, Anticancer Drugs, Chemotherapeutic Drugs, Collagen, Analysis, Physiological aspects, Genetic aspects, Antineoplastic agents, Proteolysis, Structure, Membrane, Basement, Basement membrane, Antimitotic agents

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An MT1-MMP-PDGF receptor-beta axis regulates mural cell investment of the microvasculature

Article Abstract:

MT1-MMP was identified as a PDGF-B-selective regulator of platelet-derived growth factor (PDGFR)beta-dependent signal transduction and mural cell functions by using vascular smooth muscle cells and tissues isolated from gene-targeted mice. The data obtained identified MT1-MMP as a novel proteolytic modifier of PDGF-B/PDGFR(beta) signal transduction that cooperatively regulated vessel wall architecture in vivo.

Genetic research, Vascular smooth muscle, Transduction, Transduction (Genetics)

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